BMRB Entry 6739

Title:
Solution structure of SelM from Mus musculus   PubMed: 16319061
Deposition date:
2005-07-21
Original release date:
2005-12-28
Authors:
Ferguson, A.; Labunskyy, V.; Fomenko, D.; Arac, D.; Chelliah, Y.; Amezcua, C.; Rizo, J.; Gladyshev, V.; Deisenhofer, J.
Citation:

Citation: Ferguson, A.; Labunskyy, V.; Fomenko, D.; Arac, D.; Chelliah, Y.; Amezcua, C.; Rizo, J.; Gladyshev, V.; Deisenhofer, J.. "NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of new thioredoxin-like family."  J. Biol. Chem. ., .-. (2005).

Assembly members:

Assembly members:
Selenoprotein M, polymer, 129 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: House mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology

Experimental source:

Natural source:   Common Name: House mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology

Data sets:
Data typeCount
1H chemical shifts874
13C chemical shifts534
15N chemical shifts123

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Selenoprotein M1

Entities:

Entity 1, Selenoprotein M 129 residues - Formula weight is not available

1   METTHRASNTYRARGPROASPTRPASNARG
2   LEUARGGLYLEUALAARGGLYARGVALGLU
3   THRCYSGLYGLYCYSGLNLEUASNARGLEU
4   LYSGLUVALLYSALAPHEVALTHRGLUASP
5   ILEGLNLEUTYRHISASNLEUVALMETLYS
6   HISLEUPROGLYALAASPPROGLULEUVAL
7   LEULEUSERARGASNTYRGLNGLULEUGLU
8   ARGILEPROLEUSERGLNMETTHRARGASP
9   GLUILEASNALALEUVALGLNGLULEUGLY
10   PHETYRARGLYSSERALAPROGLUALAGLN
11   VALPROPROGLUTYRLEUTRPALAPROALA
12   LYSPROPROGLUGLUALASERGLUHISASP
13   ASPLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: Selenoprotein M, [U-15N; U-13C], 1 mM; phosphate buffer 50 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6; temperature: 298 K; ionic strength: 50 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1not availablesample_cond_1
2D TOCSYsample_1not availablesample_cond_1
3D 15N-separated NOESYsample_1not availablesample_cond_1
3D 13C-separated NOESYsample_1not availablesample_cond_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v1, Delaglio - processing

NMRView v5.2.2, Johnson - data analysis

ARIA v2.0, Nilges, M. - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

REF NP_444497
SWISS-PROT Q8VHC3
GenBank AAI47334 AAK95398 AAH19742 AAI47333
DBJ BAE43252 BAE43327 BAC29028
PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks